CHROMATOGRAPHY OF SERUM PROTEINS IN NORMAL AND PATHOLOGIC SERA: THE DISTRIBUTION OF PROTEIN-BOUND CARBOHYDRATE AND CHOLESTEROL, SIDEROPHILIN, THYROXIN-BINDING PROTEIN, B12-BINDING PROTEIN, ALKALINE AND ACID PHOSPHATASES, RADIOIODINATED ALBUMIN AND MYELOMA PROTEINS

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Abstract
A modified anion-exchange (DEAE-) cellulose chromatographic procedure for the separation and characterization of serum proteins is described. This procedure has been applied to serum samples of 20, 10, 2, and 1 ml. The chromatographic fractions of normal serum were characterized by electrophoresis and by carbohydrate and cholesterol content. The usual serum electrophoretic components have been subdivided into several fractions by this chromatographic procedure, and a faster-than-albumin component has been regularly uncovered. The chromatographic distribution of siderophilin (iron-binding protein), thyroxin-binding protein, B12-binding protein, and acid and alkaline phosphatases was determined. These components were separated on the chromatogram from many proteins of similar electrophoretic mobility. The chromatographic distribution of radioiodinated human serum albumin was found to differ significantly from the distribution of native serum albumin. Chromatograms of serum obtained from patients with chronic myelocytic leukemia, carcinoma of the breast, prostatic carcinoma, and multiple myeloma are presented. Several of these differed markedly from the normal chromatograms. In one instance the myeloma protein appeared to be separable from most of the normal gamma globulin.